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Mempro™ Cell-Based DNase I-like Protein Production

Creative Biostructure now provides Mempro™ custom cell-based DNase I-like protein production service for both academic and industry applications.

The DNase I-like protein superfamily consists of three protein families according to the OPM database: the endonuclease/exonuclease/phosphatase (EEP) family, the arthropod phospholipase D family and the bacterial phosphatidylinositol-specific phospholipase C family. The EEP family is a protein structure domain that is widely found in various proteins such as magnesium dependent endonucleases and many phosphatases involved in intracellular signaling. Arthropod phospholipase D family contains phospholipases and sphingomyelinases that are found in a wide range of organisms, including viruses, bacteria, yeast, green plants and animals. Members of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) are small, water-soluble and calcium-independent enzymes that consist of a single domain folded as a (beta alpha) (8)-barrel. They are involved in the cleaving of the natural membrane lipids PI, lyso-PI, and glycosyl-PI and interact with the membrane weakly.

Mempro™ Cell-Based DNase I-like Protein Production Figure 1. The schematic structure of Sphingomyelinase D 1. (OPM Database)

Creative Biostructure now can provide high yield, high quality DNase I-like protein production service with our most advanced cell-based systems. Cell-based systems are the most widely used method in recombinant protein production programs. With years of experience in the field of recombinant soluble/membrane protein production, our science team can provide you all kind of Mempro™ cell-based systems to meet different requirements in the production of target DNase I-like proteins, including:

Mempro™ Protein Production in Bacterial Cells System;
Mempro™ Protein Production in Yeast Cells System;
Mempro™ Protein Production in Incest Cells System;
Mempro™ Protein Production in Mammalian Cells System.

With Creative Biostructure's Mempro™ membrane protein production service, your DNase I-like protein production services will be easier and your cost will become lower. Our science team will establish the optimal strategy in each case according to the characteristics of target DNase I-like protein and your special requirements. Our common first choice is the bacteria system (E. coli), which is also the most applied system. Yeast system is also a powerful tool as it combines the advantages of both prokaryotic and eukaryotic systems such as relative economic costs, single cells, and high cell densities, faster grow rates, etc. In many cases, some proteins are difficult to express in bacteria or yeast systems, or the target protein can't be modified correctly. In these cases, insect cell systems and mammalian systems should be applied. Insect cell systems are developed from transfected cells of insects. They are also combined with vectors derived from the baculovirus species AcMNPV. Mammalian cell systems, which are the most powerful methods in recombinant protein production, provide nearly-native intracellular environments for the expression of target DNase I-like protein. Cell lines derived from various mammalian cells such as CHO, COS, HEK293, BHK-21, HeLa and GH3 are widely applied for integral membrane protein production.
Creative Biostructure also provides a wide range of other custom membrane protein production services with multiple advanced technologies. Welcome to contact us for more details.

Pan C Q, Uumer J S, Herzka A, et al. Mutational analysis of human DNase I at the DNA binding interface: implications for DNA recognition, catalysis, and metal ion dependence[J]. Protein science, 1998, 7(3): 628-636.
Malicka-Błaszkiewicz M. DNase I-like activity and actin content in the liver of some vertebrates[J]. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1986, 84(2): 207-209.
C. Trometer, and P. Falson (2010). Mammalian membrane protein expression in baculovirus-infected insect cells. Methods Mol. Biol., 601: 105-117.
S. Schlegel, et al. (2013). Bacterial-based membrane protein production. Biochim. Biophys. Acta., 1843(8): 1739-1749.

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